体球的非极核中的特定地点的水化动态,由水的动态核极化形成
Brandon D Armstrong1, Jennifer Choi, Carlos López
1Department of Physics, University of California-Santa Barbara, Santa Barbara, California 93106, United States.
Journal of the American Chemical Society
|March 30, 2011
概括
阿波米球蛋白的非极性核心.
科学领域:
- 生物物理学的生物物理.
- 蛋白质动力学 蛋白质动力学
- 结构生物学是结构生物学.
背景情况:
- 蛋白质折叠涉及从非极性核心的水挤出.
- 崩的蛋白质中间状态的水化仍然是有争议的.
- 特定位置的蛋白质水合动态很难测量.
研究的目的:
- 用特定位置的分辨率研究蛋白质水合动态.
- 为了探测不同类型的阿波米oglobin状态 (化球体,原生球体,展开的) 中的水动态.
- 探索水在蛋白质折叠中间体中的作用.
主要方法:
- 在0.35 T的Overhauser动态核极化 (ODNP) 使用特定地点的氧化物旋转标签.
- 电子偏磁共振 (EPR) 用于本地极性和移动性的洞察力.
- 在apomyoglobin上的旋转标签的10 Å以内探测水的动态.
主要成果:
- 基球蛋白融球体的非极核是水合的.
- 化水在化球体中表现出显著的转化动态 (比散装水慢4-6倍).
- 原生阿波米球蛋白显示异质的水合动态,而展开状态具有快速扩散的水.
结论:
- 特定站点的ODNP是研究蛋白质水化动态的强大工具.
- 蛋白质水合动力学是折叠依赖的,并且在不同蛋白质状态之间有所不同.
- 融化球体中的内部蛋白水是动态的,挑战了以前的假设.
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